http://www.cnr.it/ontology/cnr/individuo/prodotto/ID13448
Ribosomal crystallography: Peptide bond formation and its inhibition. (Articolo in rivista)
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- Label
- Ribosomal crystallography: Peptide bond formation and its inhibition. (Articolo in rivista) (literal)
- Anno
- 2003-01-01T00:00:00+01:00 (literal)
- Alternative label
Bashan, Anat; Zarivach, Raz; Schluenzen, Frank; Agmon, Ilana; Harms, Joerg; Auerbach, Tamar; Baram, David; Berisio, Rita; Bartels, Heike; Hansen, Harly A. S.; Fucini, Paola; Wilson, Daniel; Peretz, Moshe; Kessler, Maggie; Yonath, Ada. (2003)
Ribosomal crystallography: Peptide bond formation and its inhibition.
in Biopolymers (Print)
(literal)
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- Bashan, Anat; Zarivach, Raz; Schluenzen, Frank; Agmon, Ilana; Harms, Joerg; Auerbach, Tamar; Baram, David; Berisio, Rita; Bartels, Heike; Hansen, Harly A. S.; Fucini, Paola; Wilson, Daniel; Peretz, Moshe; Kessler, Maggie; Yonath, Ada. (literal)
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- ISI Web of Science (WOS) (literal)
- Titolo
- Ribosomal crystallography: Peptide bond formation and its inhibition. (literal)
- Abstract
- Ribosomes, the universal cellular organelles catalyzing the translation of genetic code into proteins, are protein/RNA assemblies, with a mol. wt. of ³2.5 mDa. They are composed of 2 subunits that assoc. for performing protein biosynthesis. The large subunit creates the peptide bond and provides the path for emerging proteins. The small subunit has key roles in initiating the process and controlling its fidelity. Crystallog. studies on complexes of the small and the large eubacterial ribosomal subunits with substrate analogs, antibiotics, and inhibitors have confirmed that rRNA governs most of its activities and have indicated that the main catalytic contribution of the ribosome is the precise positioning and alignment of its substrates, the tRNA mols. A symmetry-related region of significant size, contg. .apprx.200 nucleotides, has been revealed in all known structures of the large ribosomal subunit, despite the asym. nature of the ribosome. The symmetry rotation axis, identified in the middle of the peptide bond-formation site, coincides with the bond connecting the tRNA double-helical features with its single-stranded 3' end, which is the moiety carrying the amino acids. This implies sovereign movements of tRNA features and suggests that tRNA translocation involves a rotatory motion within the ribosome active site. This motion is guided and anchored by ribosomal nucleotides belonging to the active site walls, and results in geometry suitable for peptide bond formation with no significant rearrangements. The sole geometric requirement for the proposed mechanism is that the initial P-site tRNA adopts the flipped orientation. The rotatory motion is the major component of unified machinery for peptide bond formation, translocation, and nascent protein progression, since its spiral nature ensures the entrance of the nascent peptide into the ribosomal exit tunnel.
This tunnel, assumed to be a passive path for the growing chains, has been found to be involved dynamically in gating and discrimination (literal)
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